Screening of novel feruloyl esterases from Talaromyces wortmannii for the development of efficient and sustainable syntheses of feruloyl derivatives
| Autor: | Laura Iancu, Peter Jütten, Ulrika Rova, Alexander Piechot, Paul Christakopoulos, Io Antonopoulou |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0106 biological sciences
0301 basic medicine Arabinose Vinyl Compounds Coumaric Acids Bioconversion Bioengineering 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Prenol Substrate Specificity 03 medical and health sciences Hydrolysis chemistry.chemical_compound Hemiterpenes Pentanols Feruloyl esterase 010608 biotechnology Organic chemistry Esterification Chemistry Substrate (chemistry) Transesterification 030104 developmental biology Talaromyces Yield (chemistry) Solvents Carboxylic Ester Hydrolases Biotechnology |
| Zdroj: | Enzyme and microbial technology. 120 |
| ISSN: | 1879-0909 |
| Popis: | The feruloyl esterases Fae125, Fae7262 and Fae68 from Talaromyces wortmannii were screened in 10 different solvent: buffer systems in terms of residual hydrolytic activity and of the ability for the transesterification of vinyl ferulate with prenol or l -arabinose. Among the tested enzymes, the acetyl xylan-related Fae125 belonging to the phylogenetic subfamily 5 showed highest yield and selectivity for both products in alkane: buffer systems (n-hexane or n-octane). Response surface methodology, based on a 5-level and 6-factor central composite design, revealed that the substrate molar ratio and the water content were the most significant variables for the bioconversion yield and selectivity. The effect of agitation, the possibility of DMSO addition and the increase of donor concentration were investigated. After optimization, competitive transesterification yields were obtained for prenyl ferulate (87.5–92.6%) and l -arabinose ferulate (56.2–61.7%) at reduced reaction times (≤24 h) resulting in good productivities (>1 g/L/h, >300 kg product/kg FAE). The enzyme could be recycled for six consecutive cycles retaining 66.6% of the synthetic activity and 100% of the selectivity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect